High-resolution crystals of the HU mutant K38N from Bacillus stearothermophilus

Takahiro Tominaga, Atsushi Nakagawa, Isao Tanaka, Shunsuke Kawamura, Makoto Kimura

研究成果: ジャーナルへの寄稿学術誌査読

1 被引用数 (Scopus)

抄録

The DNA-binding protein HU is ubiquitous in the prokaryotic cell. It is a major protein component of isolated nucleoids and is believed to control the tertiary structure of prokaryotic DNA. The Bacillus stearothermophilus HU (BstHU) mutants obtained by mutagenesis have been investigated. Crystallization experiments of BstHU-K38N (Lys38 is substituted with Asn) resulted in two forms of crystals suitable for high-resolution x-ray analysis. The first form belongs to the monoclinic space group C2 with unit- cell dimensions of a = 90.1 Å, b = 43.5 Å, c = 63.7 Å, and β = 135.1°and it diffracts x rays to 1.5-Å resolution. The second form belongs to the tetragonal space group I41 with a = b = 62.6 Å and c = 43.3 Å, and it diffracts up to 1.8-Å resolution.

本文言語英語
ページ(範囲)86-89
ページ数4
ジャーナルJournal of structural biology
125
1
DOI
出版ステータス出版済み - 3月 1999

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学

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